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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Endophilin regulates JNK activation through its interaction with the germinal center kinase-like kinase.

The endophilin family of proteins function in clathrin-mediated endocytosis. Here, we have identified and cloned the rat germinal center kinase-like kinase (rGLK), a member of the GCK (germinal center kinase) family of c-Jun N-terminal kinase ( JNK) activating enzymes, as a novel endophilin I-binding partner. The interaction occurs both in vitro and in cells and is mediated by the Src homology 3 domain of endophilin I and a region of rGLK containing the endophilin consensus-binding sequence PPRPPPPR. Overlay analysis of rat brain extracts demonstrates that endophilin I is a major Src homology 3 domain-binding partner for rGLK. Overexpression of full-length endophilin I activates rGLK- mediated JNK activation, whereas N- and C-terminal fragments of endophilin I block JNK activation. Thus, endophilin I appears to have a novel function in JNK activation.[1]

References

  1. Endophilin regulates JNK activation through its interaction with the germinal center kinase-like kinase. Ramjaun, A.R., Angers, A., Legendre-Guillemin, V., Tong, X.K., McPherson, P.S. J. Biol. Chem. (2001) [Pubmed]
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